ID   KI21A_MOUSE             Reviewed;        1672 AA.
AC   Q9QXL2; Q6P5H1; Q6ZPJ8; Q8BWZ9; Q8BXF1;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=Kinesin-like protein KIF21A;
GN   Name=Kif21a; Synonyms=Kiaa1708;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=10225949; DOI=10.1083/jcb.145.3.469;
RA   Marszalek J.R., Weiner J.A., Farlow S.J., Chun J., Goldstein L.S.;
RT   "Novel dendritic kinesin sorting identified by different process targeting
RT   of two related kinesins: KIF21A and KIF21B.";
RL   J. Cell Biol. 145:469-479(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-551, AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1129-1672 (ISOFORM 4).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 382-1672 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1660 AND SER-1671, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-1660 AND SER-1671,
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1101; SER-1102 AND SER-1207
RP   (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Microtubule-binding motor protein probably involved in
CC       neuronal axonal transport. In vitro, has a plus-end directed motor
CC       activity. {ECO:0000269|PubMed:10225949}.
CC   -!- SUBUNIT: Interacts (via residues 1148-1169) with KANK1 (via ankyrin
CC       repeats 1-5) and KANK2 (via ankyrin repeats 1-5).
CC       {ECO:0000250|UniProtKB:Q7Z4S6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:10225949}. Cell projection, dendrite
CC       {ECO:0000269|PubMed:10225949}. Cell projection, axon
CC       {ECO:0000269|PubMed:10225949}. Note=In neurons, localized to axons and
CC       dendrites. {ECO:0000269|PubMed:10225949}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9QXL2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9QXL2-2; Sequence=VSP_010873, VSP_010874, VSP_010875;
CC       Name=3;
CC         IsoId=Q9QXL2-3; Sequence=VSP_010873, VSP_010876;
CC       Name=4;
CC         IsoId=Q9QXL2-4; Sequence=VSP_010877;
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in brain.
CC       {ECO:0000269|PubMed:10225949}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR   EMBL; AF202892; AAF17083.1; -; mRNA.
DR   EMBL; BC060698; AAH60698.1; -; mRNA.
DR   EMBL; BC062896; AAH62896.1; -; mRNA.
DR   EMBL; AK129426; BAC98236.1; -; mRNA.
DR   EMBL; AK049303; BAC33669.1; -; mRNA.
DR   EMBL; AK047350; BAC33031.1; -; mRNA.
DR   CCDS; CCDS37179.1; -. [Q9QXL2-2]
DR   CCDS; CCDS49706.1; -. [Q9QXL2-3]
DR   CCDS; CCDS49708.1; -. [Q9QXL2-1]
DR   RefSeq; NP_001102510.1; NM_001109040.2. [Q9QXL2-1]
DR   RefSeq; NP_001102511.1; NM_001109041.2.
DR   RefSeq; NP_001102512.1; NM_001109042.2. [Q9QXL2-3]
DR   RefSeq; NP_057914.2; NM_016705.4. [Q9QXL2-2]
DR   PDB; 5YAY; X-ray; 1.55 A; B=1142-1169.
DR   PDB; 5YBE; X-ray; 2.11 A; B=1151-1169.
DR   PDBsum; 5YAY; -.
DR   PDBsum; 5YBE; -.
DR   AlphaFoldDB; Q9QXL2; -.
DR   SMR; Q9QXL2; -.
DR   BioGRID; 200939; 8.
DR   IntAct; Q9QXL2; 7.
DR   MINT; Q9QXL2; -.
DR   STRING; 10090.ENSMUSP00000085985; -.
DR   GlyGen; Q9QXL2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9QXL2; -.
DR   PhosphoSitePlus; Q9QXL2; -.
DR   SwissPalm; Q9QXL2; -.
DR   MaxQB; Q9QXL2; -.
DR   PaxDb; 10090-ENSMUSP00000085985; -.
DR   PeptideAtlas; Q9QXL2; -.
DR   ProteomicsDB; 264749; -. [Q9QXL2-1]
DR   ProteomicsDB; 264750; -. [Q9QXL2-2]
DR   ProteomicsDB; 264751; -. [Q9QXL2-3]
DR   ProteomicsDB; 264752; -. [Q9QXL2-4]
DR   Pumba; Q9QXL2; -.
DR   Antibodypedia; 13055; 79 antibodies from 22 providers.
DR   DNASU; 16564; -.
DR   Ensembl; ENSMUST00000088614.13; ENSMUSP00000085985.6; ENSMUSG00000022629.18. [Q9QXL2-1]
DR   Ensembl; ENSMUST00000109287.4; ENSMUSP00000104910.3; ENSMUSG00000022629.18. [Q9QXL2-3]
DR   Ensembl; ENSMUST00000109288.9; ENSMUSP00000104911.3; ENSMUSG00000022629.18. [Q9QXL2-2]
DR   GeneID; 16564; -.
DR   KEGG; mmu:16564; -.
DR   UCSC; uc007xhs.3; mouse. [Q9QXL2-1]
DR   UCSC; uc007xht.3; mouse. [Q9QXL2-2]
DR   UCSC; uc007xhv.3; mouse. [Q9QXL2-3]
DR   AGR; MGI:109188; -.
DR   CTD; 55605; -.
DR   MGI; MGI:109188; Kif21a.
DR   VEuPathDB; HostDB:ENSMUSG00000022629; -.
DR   eggNOG; KOG0244; Eukaryota.
DR   GeneTree; ENSGT00940000155323; -.
DR   HOGENOM; CLU_001485_4_5_1; -.
DR   InParanoid; Q9QXL2; -.
DR   OrthoDB; 1131899at2759; -.
DR   PhylomeDB; Q9QXL2; -.
DR   TreeFam; TF105224; -.
DR   Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   Reactome; R-MMU-983189; Kinesins.
DR   BioGRID-ORCS; 16564; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Kif21a; mouse.
DR   PRO; PR:Q9QXL2; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q9QXL2; Protein.
DR   Bgee; ENSMUSG00000022629; Expressed in habenula and 245 other cell types or tissues.
DR   ExpressionAtlas; Q9QXL2; baseline and differential.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0071532; F:ankyrin repeat binding; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   CDD; cd01372; KISc_KIF4; 1.
DR   CDD; cd22263; Rcc_KIF21A; 1.
DR   CDD; cd00200; WD40; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR027640; Kinesin-like_fam.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR   PANTHER; PTHR47969:SF30; KINESIN MOTOR DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF00400; WD40; 5.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF46579; Prefoldin; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR   Genevisible; Q9QXL2; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW   Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW   Motor protein; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Repeat; WD repeat.
FT   CHAIN           1..1672
FT                   /note="Kinesin-like protein KIF21A"
FT                   /id="PRO_0000125463"
FT   DOMAIN          9..371
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REPEAT          1343..1380
FT                   /note="WD 1"
FT   REPEAT          1383..1421
FT                   /note="WD 2"
FT   REPEAT          1447..1485
FT                   /note="WD 3"
FT   REPEAT          1488..1530
FT                   /note="WD 4"
FT   REPEAT          1539..1576
FT                   /note="WD 5"
FT   REPEAT          1580..1619
FT                   /note="WD 6"
FT   REPEAT          1622..1659
FT                   /note="WD 7"
FT   REGION          556..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          780..808
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          836..886
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1109..1139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1148..1169
FT                   /note="Interaction with KANK1 and KANK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z4S6"
FT   REGION          1172..1315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          365..840
FT                   /evidence="ECO:0000255"
FT   COILED          933..1021
FT                   /evidence="ECO:0000255"
FT   COILED          1055..1085
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        558..603
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..637
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        850..882
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1222..1237
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1239..1266
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1282..1307
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         88..95
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z4S6"
FT   MOD_RES         258
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         524
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z4S6"
FT   MOD_RES         1227
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z4S6"
FT   MOD_RES         1231
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z4S6"
FT   MOD_RES         1241
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z4S6"
FT   MOD_RES         1660
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1662
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z4S6"
FT   MOD_RES         1671
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         558..570
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:10225949,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_010873"
FT   VAR_SEQ         1109..1115
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10225949"
FT                   /id="VSP_010874"
FT   VAR_SEQ         1226..1305
FT                   /note="ISRQSSLSEKKVPEPSPVTRRKAYEKADKPKAKEHKHSDSGASETSLSPPSS
FT                   PPSRPRNELNVFNRLTVPQGTPSVQQDK -> M (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10225949"
FT                   /id="VSP_010875"
FT   VAR_SEQ         1227..1318
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_010876"
FT   VAR_SEQ         1262..1318
FT                   /note="HSDSGASETSLSPPSSPPSRPRNELNVFNRLTVPQGTPSVQQDKSDESDSSL
FT                   SEVHR -> Q (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_010877"
FT   CONFLICT        1127
FT                   /note="P -> A (in Ref. 1; AAF17083)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1311
FT                   /note="S -> F (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1321
FT                   /note="I -> L (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   HELIX           1155..1157
FT                   /evidence="ECO:0007829|PDB:5YAY"
FT   HELIX           1162..1166
FT                   /evidence="ECO:0007829|PDB:5YAY"
FT   MOD_RES         Q9QXL2-2:1101
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         Q9QXL2-2:1102
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         Q9QXL2-2:1207
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   1672 AA;  186536 MW;  1B2480E5129105AB CRC64;
     MLGAADESSV RVAVRIRPQL AKEKIEGCHI CTSVTPGEPQ VFLGKDKAFT FDYVFDIDSQ
     QEQIYTQCIE KLIEGCFEGY NATVFAYGQT GAGKTYTMGT GFDVNIMEEE QGIISRAVRH
     LFKSIDEKKT SAIKNGLPPP EFKVNAQFLE LYNEEVLDLF DTTRDIDAKN KKSNIRIHED
     STGGIYTVGV TTRTVNTEPE MMQCLKLGAL SRTTASTQMN VQSSRSHAIF TIHVCQTRVC
     PQTDAENATD NKLISESSPM NEFETLTAKF HFVDLAGSER LKRTGATGER AKEGISINCG
     LLALGNVISA LGDKSKRATH VPYRDSKLTR LLQDSLGGNS QTIMIACVSP SDRDFMETLN
     TLKYANRARN IKNKVMVNQD RASQQINALR SEITRLQMEL MEYKTGKRII DEEGVESIND
     MFHENAMLQT ENNNLRVRIK AMQETVDALR ARITQLVSEQ ANQVLARAGE GNEEISNMIH
     SYIKEIEDLR AKLLESEAVN ENLRKNLTRA TARSPYFSAS SAFSPTILSS DKETIEIIDL
     AKKDLEKLKR KEKKKKKRLQ KLEESGREER SVAGKDDNAD TDQEKKEEKG VSEKENNELD
     VEENQEVSDH EDEEEEEEDE EEEDDIEGEE SSDESDSESD EKANYQADLA NITCEIAIKQ
     KLIDELENSQ KRLQTLKKQY EEKLMMLQHK IRDTQLERDQ VLQNLGSVES YSEEKAKKVK
     CEYEKKLHAM NKELQRLQTA QKEHARLLKN QSQYEKQLKK LQQDVMEMKK TKVRLMKQMK
     EEQEKARLTE SRRNREIAQL KKDQRKRDHQ LRLLEAQKRN QEVVLRRKTE EVTALRRQVR
     PMSDKVAGKV TRKLSSSESP APDTGSSAAS GEADTSRPGT QQKMRIPVAR VQALPTPTTN
     GTRKKYQRKG FTGRVFTSKT ARMKWQLLER RVTDIIMQKM TISNMEADMN RLLRQREELT
     KRREKLSKRR EKIVKESGEG DKSVANIIEE MESLTANIDY INDSIADCQA NIMQMEEAKE
     EGETLDVTAV INACTLTEAR YLLDHFLSMG INKGLQAAQK EAQIKVLEGR LKQTEITSAT
     QNQLLFHMLK EKAELNPELD ALLGHALQDL DGAPPENEED SSEEDGPLHS PGSEGSTLSS
     DLMKLCGEVK PKNKARRRTT TQMELLYADS SEVASDTSAG DASLSGPLAP VAEGQEIGMN
     TETSGTSARD KELLAPSGLP SKIGSISRQS SLSEKKVPEP SPVTRRKAYE KADKPKAKEH
     KHSDSGASET SLSPPSSPPS RPRNELNVFN RLTVPQGTPS VQQDKSDESD SSLSEVHRGI
     INPFPACKGV RASPLQCVHI AEGHTKAVLC VDSTDDLLFT GSKDRTCKVW NLVTGQEIMS
     LGVHPNNVVS VKYCNYTSLV FTVSTSYIKV WDIRESAKCI RTLTSSGQVT LGEACSASTS
     RTVAIPSGES QINQIALNPT GTFLYAASGN AVRMWDLKRF QSTGKLTGHL GPVMCLTVDQ
     ISNGQDLIIT GSKDHYIKMF DVTEGALGTV SPTHNFEPPH YDGIEALAIQ GDNLFSGSRD
     NGIKKWDLAQ KGLLQQVPNA HKDWVCALGL VPGHPVLLSG CRGGILKLWN VDTFVPVGEM
     RGHDSPINAI CVNSTHVFTA ADDRTVRIWK AHNLQDGQLS DTGDLGEDIA SN
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